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G. Lalmanach, J. Hoebeke, T. Moreau, M. Martino, F. Gauthier (1992)
An immunochemical approach to investigating the mechanism of inhibition of cysteine proteinases by members of the cystatin superfamily.Journal of immunological methods, 149 2
H. Nawa, N. Kitamura, T. Hirose, M. Asai, S. Inayama, S. Nakanishi (1983)
Primary structures of bovine liver low molecular weight kininogen precursors and their two mRNAs.Proceedings of the National Academy of Sciences of the United States of America, 80 1
S. Furuto-Kato, A. Matsumoto, N. Kitamura, S. Nakanishi (1985)
Primary structures of the mRNAs encoding the rat precursors for bradykinin and T-kinin. Structural relationship of kininogens with major acute phase protein and alpha 1-cysteine proteinase inhibitor.The Journal of biological chemistry, 260 22
N. Gutman, T. Moreau, F. Alhenc-Gelas, T. Baussant, A. Moujahed, S. Akpona, F. Gauthier (1988)
T-kinin release from T-kininogen by rat-submaxillary-gland endopeptidase K.European journal of biochemistry, 171 3
Heiko Herwald, Mattias Collin, W. Miiller-Esterl, Ears Bj6rck (1996)
Streptococcal cysteine proteinase releases kinins: a virulence mechanismThe Journal of Experimental Medicine, 184
K. Bhoola, C. Figueroa, K. Worthy (1992)
Bioregulation of kinins: kallikreins, kininogens, and kininases.Pharmacological reviews, 44 1
M. Brillard-Bourdet, T. Moreau, F. Gauthier (1995)
Substrate specificity of tissue kallikreins: importance of an extended interaction site.Biochimica et biophysica acta, 1246 1
B. Lenarčič, T. Bevec (1998)
Thyropins--new structurally related proteinase inhibitors.Biological chemistry, 379 2
W. Machleidt, D. Nägler, I. Assfalg‐Machleidt, M. Stubbs, H. Fritz, E. Auerswald (1995)
Temporary inhibition of papain by hairpin loop mutants of chicken cystatin Distorted binding of the loops results in cleavage of the Gly9‐Ala10 bondFEBS Letters, 361
B. Turk, D. Turk, V. Turk (2000)
Lysosomal cysteine proteases: more than scavengers.Biochimica et biophysica acta, 1477 1-2
T. Popović, N. Cimerman, I. Dolenc, A. Ritonja, J. Brzin (1999)
Cathepsin L is capable of truncating cystatin C of 11 N‐terminal amino acidsFEBS Letters, 455
Y. Takagaki, N. Kitamura, S. Nakanishi (1985)
Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens.The Journal of biological chemistry, 260 14
Wolfram Bode, R. Huber (1992)
Natural protein proteinase inhibitors and their interaction with proteinases.European journal of biochemistry, 204 2
W. Machleidt, U. Thiele, B. Laber, I. Assfalg‐Machleidt, A. Esterl, G. Wiegand, J. Kos, V. Turk, W. Bode (1989)
Mechanism of inhibition of papain by chicken egg white cystatinFEBS Letters, 243
A. Barrett, A. Kembhavi, Molly Brown, H. Kirschke, C. Knight, Masaharu TAMAIt, Kazunori HANADAt (1982)
L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.The Biochemical journal, 201 1
A. Adam, A. Albert, G. Calay, J. Closset, J. Damas, P. Franchimont (1985)
Human kininogens of low and high molecular mass: quantification by radioimmunoassay and determination of reference values.Clinical chemistry, 31 3
D. Michaud, L. Cantin, D. Raworth, T. Vrain (1996)
Assessing the stability of cystatin/cysteine proteinase complexes using mildly‐denaturing gelatin‐polyacrylamide gel electrophoresisELECTROPHORESIS, 17
J. Scharfstein, V. Schmitz, V. Morandi, M. Capella, A. Lima, A. Morrot, L. Juliano, W. Müller-Esterl (2000)
Host Cell Invasion by TRYPANOSOMA cRUZI Is Potentiated by Activation of Bradykinin B2 ReceptorsThe Journal of Experimental Medicine, 192
E. Nery, M. Juliano, A. Lima, J. Scharfstein, L. Juliano (1997)
Kininogenase Activity by the Major Cysteinyl Proteinase (Cruzipain) from Trypanosoma cruzi *The Journal of Biological Chemistry, 272
A. Baron, A. Decarlo, J. Featherstone (2008)
Functional aspects of the human salivary cystatins in the oral environment.Oral diseases, 5 3
R. Pike, T. Coetzer, C. Dennison (1992)
Proteolytically active complexes of cathepsin L and a cysteine proteinase inhibitor; purification and demonstration of their formation in vitro.Archives of biochemistry and biophysics, 294 2
A. Anastasi, M. Brown, A. Kembhavi, M. Nicklin, C. Sayers, D. Sunter, A. Barrett (1983)
Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum.The Biochemical journal, 211 1
M. Mcgrath (1999)
The lysosomal cysteine proteases.Annual review of biophysics and biomolecular structure, 28
M. Wiser, J. Lonsdale-Eccles, A. D'alessandro, D. Grab (1997)
A cryptic protease activity from Trypanosoma cruzi revealed by preincubation with kininogen at low temperatures.Biochemical and biophysical research communications, 240 3
B. Turk, Turk, D. Turk (1997)
Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors.Biological chemistry, 378 3-4
Boris Turk, I. Dolenc, Vito Turk, Joseph Bieth (1993)
Kinetics of the pH-induced inactivation of human cathepsin L.Biochemistry, 32 1
G. Salvesen, C. Parkes, M. Abrahamson, A. Grubb, A. Barrett (1986)
Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.The Biochemical journal, 234 2
G. Lalmanach, A. Adam, T. Moreau, N. Gutman, F. Gauthier (1991)
Discrimination between rat thiostatin (T-kininogen) and one of its cystatin-like inhibitory fragments by a monoclonal antibody, and localization of the epitope.European journal of biochemistry, 196 1
Abstract Although papainlike enzymes are strongly inhibited by their natural tightbinding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward ZPheArgAMC in the presence of an excess of kininogen. This activity is abolished by adding E-64 or chicken cystatin. Cathepsins B and L show a single band of gelatinolytic activity when subjected to gelatinSDSPAGE. Adding high M kininogen, low M kininogen, Tkininogen, or chicken cystatin to cathepsin L results in additional intense bands of enzyme activity corresponding to the proteaseinhibitor complexes. Cathepsin B does not produce these additional bands. This gelatinolytic activity was inhibited by E-64, but not by EDTA, PMSF or Pefabloc. Cathepsin L also specifically generated kinins from high and low molecular weight kininogens in vitro, but cathepsin B did not. Tkininogen did not release any immunoreactive kinins when complexed with cathepsin L, as previously observed using tissue kallikreins. The ability of cathepsin L to generate vasoactive peptides raises the question of the physiological significance of this mechanism during inflammation.
Biological Chemistry – de Gruyter
Published: May 5, 2001
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